A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Structural characterization of three noncanonical NTF2-like superfamily proteins: implications for polyketide biosynthesis
Tekijät: N. Vuksanovic, X. Zhu, D.A. Serrano, V. Siitonen, M. Metsä-Ketelä, C.E. Melancon III, N.R. Silvaggi
Kustantaja: INT UNION CRYSTALLOGRAPHY
Julkaisuvuosi: 2020
Journal: Acta Crystallographica Section F: Structural Biology Communications
Tietokannassa oleva lehden nimi: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Lehden akronyymi: ACTA CRYSTALLOGR F
Vuosikerta: 76
Aloitussivu: 372
Lopetussivu: 383
Sivujen määrä: 12
eISSN: 2053-230X
DOI: https://doi.org/10.1107/S2053230X20009814
Rinnakkaistallenteen osoite: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397469
Proteins belonging to the NTF2-like superfamily are present in the biosynthetic pathways of numerous polyketide natural products, such as anthracyclins and benzoisochromanequinones. Some have been found to be bona fide polyketide cyclases, but many of them have roles that are currently unknown. Here, the X-ray crystal structures of three NTF2-like proteins of unknown function are reported: those of ActVI-ORFA from Streptomyces coelicolor A3(2) and its homologs Caci_6494, a protein from an uncharacterized biosynthetic cluster in Catenulispora acidiphila, and Aln2 from Streptomyces sp. CM020, a protein in the biosynthetic pathway of alnumycin. The presence of a solvent-accessible cavity and the conservation of the His/Asp dyad that is characteristic of many polyketide cyclases suggest a potential enzymatic role for these enzymes in polyketide biosynthesis.
